title: NMR solution structure of the neurotrypsin Kringle domain.
abstract: Neurotrypsin is a multidomain protein that serves as a brain-specific serine protease. Here we report the NMR structure of its kringle domain, NT/K. The data analysis was performed with the BACUS (Bayesian analysis of coupled unassigned spins) algorithm. This study presents the first application of BACUS to the structure determination of a 13C unenriched protein for which no prior experimental 3D structure was available. NT/K adopts the kringle fold, consisting of an antiparallel beta-sheet bridged by an overlapping pair of disulfides. The structure reveals the presence of a surface-exposed left-handed polyproline II helix that is closely packed to the core beta-structure. This feature distinguishes NT/K from other members of the kringle fold and points toward a novel functional role for a kringle domain. Functional divergence among kringle domains is discussed on the basis of their surface and electrostatic characteristics.
authors.affiliation: Department of Chemistry, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213, USA. oao.sputnik@gmail.com
authors.forename: Olga A
authors.initials: OA
authors.lastname: Ozhogina
authors.forename: Alexander
authors.initials: A
authors.lastname: Grishaev
authors.forename: Emile L
authors.initials: EL
authors.lastname: Bominaar
authors.forename: László
authors.initials: L
authors.lastname: Patthy
authors.forename: Maria
authors.initials: M
authors.lastname: Trexler
authors.forename: Miguel
authors.initials: M
authors.lastname: Llinás
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001499:Bayes Theorem; D018082:Kringles; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D051381:Rats; D016415:Sequence Alignment; D012697:Serine Endopeptidases / Q000737:chemistry*; D012996:Solutions
chemical_list: D012996:Solutions; D012697:Serine Endopeptidases; C108493:neurotrypsin